On the nature of rat hepatic and mouse olfactory sulfotransferases

Michio Matsui, Hiroomi Tamura, Fusako Nagai, Hiroshi Homma, Atsushi Miyawaki, Katsuhiko Mikoshiba

Research output: Contribution to journalArticle

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Abstract

Rat hydroxysteroid sulfotransferase (HS-SULT) cDNAs, ST-40 and ST-20 are 90% identical in amino acid sequences and show different substrate specificities toward dehydroepiandrosterone (DHEA), androsterone (AD) and cortisol (CS). ST-40 enzyme is active toward the three substrates, whereas ST-20 enzyme is preferentially active for CS. First we prepared mutants of well conserved histidine, lysine and asparagine by site-directed mutagenesis. Secondly we constructed 20 chimeric HS-SULTs by reciprocal exchange of five protein domains between ST-20 and ST-40 enzymes. The studies on the expressed mutant and chimetic enzymes indicate the importance of the C-terminal region for the substrate specificity and the involvement of multiple regions for the enzyme activities. Next we determined the genetic loci of ST-40 and ST-20 by fluorescence in situ hybridization. Biotinylated ST-20 and ST-40 probes gave a pair of fluorescent spots on the same region of rat chromosome 1 and the loci of these genes were localized to the same chromosomal region of 1q21.3→q22.1. Finally we studied mouse olfactory phenol SULT (P-SULT). It was immunolocalized in the cytoplasm of mouse olfactory sustentacular cells and mouse nasal cytosols show high SULT activities toward phenolic aromatic odorants. We subsequently isolated a mouse P-SULT cDNA from mouse olfactory cDNA library. It encodes 304 amino acid polypeptide and is 94% identical with rat STlC1 in amino acid sequences.

Original languageEnglish
Pages (from-to)69-80
Number of pages12
JournalChemico-Biological Interactions
Volume109
Issue number1-3
DOIs
Publication statusPublished - 1998 Feb 20

Fingerprint

Sulfotransferases
Rats
Liver
Enzymes
Phenol
Amino Acids
Hydrocortisone
Substrate Specificity
Substrates
Complementary DNA
Androsterone
Amino Acid Sequence
Mutagenesis
Dehydroepiandrosterone
Asparagine
Enzyme activity
Chromosomes
Gene Library
Histidine
Genetic Loci

Keywords

  • Dehydroepiandrosterone
  • Enzymes
  • Sulfotransferase

ASJC Scopus subject areas

  • Toxicology

Cite this

On the nature of rat hepatic and mouse olfactory sulfotransferases. / Matsui, Michio; Tamura, Hiroomi; Nagai, Fusako; Homma, Hiroshi; Miyawaki, Atsushi; Mikoshiba, Katsuhiko.

In: Chemico-Biological Interactions, Vol. 109, No. 1-3, 20.02.1998, p. 69-80.

Research output: Contribution to journalArticle

Matsui, Michio ; Tamura, Hiroomi ; Nagai, Fusako ; Homma, Hiroshi ; Miyawaki, Atsushi ; Mikoshiba, Katsuhiko. / On the nature of rat hepatic and mouse olfactory sulfotransferases. In: Chemico-Biological Interactions. 1998 ; Vol. 109, No. 1-3. pp. 69-80.
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